Figure 4.
Figure 4 (A) RIBBONS diagram of DnaA and p97 (residues
191−458) showing the high degree of structural conservation
across the AAA+ domain of the two proteins (the r.m.s.d. between
the two proteins is 3.2 Å over 192 C[ ]positions).
(B) RIBBONS diagram of the AAA+ region of a p97 dimer excised
from the hexameric structure (inset) (Zhang et al., 2000)
depicting the typical oligomeric arrangement of AAA+ protomers.
The ADP bound at the interface is shown in black. The helix
containing the Box VII motif is shown in cyan and the key
arginine residue present at the dimerization interface is
depicted as a magenta ball-and-stick model. (C) Inset: surface
depiction (Nicholls et al., 1991) of the DnaA dimer modeled on
p97, showing the high degree of complementarity between the
monomers. The structural alignment of the AAA+ regions was
generated using least-squares fitting of the DnaA AAA+ domain on
each of two neighboring p97 AAA+ domains from the p97 hexamer.
The exploded view reveals the clustering of conserved residues
at the dimerization interface to form the bipartite
nucleotide-interaction site. The degree of conservation among
all known DnaA sequences is indicated by the degree of blue
shading (Figure 1B); invariant (magenta) and chemically
conserved residues (pink) are also highlighted. (D) RIBBONS
diagram of the DnaA AAA+ domain (residues D77^S130−G290^N348)
model dimer shown in blue and gold. Critical elements present at
the predicted dimer interface are highlighted as in Figure 4B.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2002,
21,
4763-4773)
copyright 2002.
]positions).
(B) RIBBONS diagram of the AAA+ region of a p97 dimer excised
from the hexameric structure (inset) (Zhang et al., 2000)
depicting the typical oligomeric arrangement of AAA+ protomers.
The ADP bound at the interface is shown in black. The helix
containing the Box VII motif is shown in cyan and the key
arginine residue present at the dimerization interface is
depicted as a magenta ball-and-stick model. (C) Inset: surface
depiction (Nicholls et al., 1991) of the DnaA dimer modeled on
p97, showing the high degree of complementarity between the
monomers. The structural alignment of the AAA+ regions was
generated using least-squares fitting of the DnaA AAA+ domain on
each of two neighboring p97 AAA+ domains from the p97 hexamer.
The exploded view reveals the clustering of conserved residues
at the dimerization interface to form the bipartite
nucleotide-interaction site. The degree of conservation among
all known DnaA sequences is indicated by the degree of blue
shading (Figure 1B); invariant (magenta) and chemically
conserved residues (pink) are also highlighted. (D) RIBBONS
diagram of the DnaA AAA+ domain (residues D77^S130−G290^N348)
model dimer shown in blue and gold. Critical elements present at
the predicted dimer interface are highlighted as in Figure 4B.